Advances in protein engineering and biotechnology, have led to large scale production of proteins and peptides for pharmaceutical purposes such as replacement therapies and vaccines. However, due to their complex structure and folding dynamics, proteins undergo physical and chemical instability. These instabilities present unique difficulties in the production, formulation, storage and administration of protein pharmaceuticals (1,2). Chemical instability is related to covalent modification of the protein that leads to loss of activity. One strategy to overcome this difficulty and to prolong the shelf life, is to freeze dry protein products and reconstitute them prior to the administration. The reconstitution buffer is generally provided by the manufacturer. However, unique handling procedures need to be followed to avoid physical instability, as the reconstitution involves agitation, formation of foam and froth and the exposure of proteins to air-aqueous interface. Physical instability is related to protein folding at the molecular level, and denaturation, surface adsorption, aggregation, and precipitation are frequent manifestations of physical instability (1-3). Such instabilities complicate the safety of protein products as the presence of aggregates evokes undesired immune response (4). The loss of protein due to surface adsorption and binding to vial and syringes complicates the therapy. In order to avoid surface adsorption, it is a general practice to include large quantities of albumin but inclusion of such excipients presents other pharmaceutical problems including the safety related to the source of albumin.